PMID:15736961
| Citation |
Ramakrishnan, M, Qu, J, Pocanschi, CL, Kleinschmidt, JH and Marsh, D (2005) Orientation of beta-barrel proteins OmpA and FhuA in lipid membranes. Chain length dependence from infrared dichroism. Biochemistry 44:3515-23 |
|---|---|
| Abstract |
The outer-membrane proteins OmpA and FhuA of Escherichia coli are monomeric beta-barrels of widely differing size. Polarized attenuated total reflection infrared spectroscopy has been used to determine the orientation of the beta-barrels in phosphatidylcholine host matrices of different lipid chain lengths. The linear dichroism of the amide I band from OmpA and FhuA in hydrated membranes generally increases with increasing chain length from diC(12:0) to diC(17:0) phosphatidylcholine, in both the fluid and gel phases. Measurements of the amide I and amide II dichroism from dry samples are used to deduce the strand tilt (beta = 46 degrees for OmpA and beta = 44.5 degrees for FhuA). These values are then used to deduce the order parameters, P(2)(cos alpha), of the beta-barrels from the amide I dichroic ratios of the hydrated membranes. The orientational ordering of the beta-barrels and their assembly in the membrane are discussed in terms of hydrophobic matching with the lipid chains. |
| Links |
PubMed Online version:10.1021/bi047603y |
| Keywords |
Amides; Bacterial Outer Membrane Proteins/chemistry; Bacterial Outer Membrane Proteins/metabolism; Cell Membrane/chemistry; Cell Membrane/metabolism; Circular Dichroism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/metabolism; Hydrophobic and Hydrophilic Interactions; Iron/chemistry; Iron/metabolism; Lipid Bilayers/chemistry; Membrane Lipids/chemistry; Models, Chemical; Phosphatidylcholines/chemistry; Protein Structure, Secondary; Receptors, Cell Surface/chemistry; Receptors, Cell Surface/metabolism; Receptors, Virus/chemistry; Receptors, Virus/metabolism |
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